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Gene Review

ECs1859  -  exoribonuclease II

Escherichia coli O157:H7 str. Sakai

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Disease relevance of ECs1859


High impact information on ECs1859

  • Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins [5].
  • RNase II is a member of the widely distributed RNR family of exoribonucleases, which are highly processive 3'-->5' hydrolytic enzymes that play an important role in mRNA decay [1].
  • The putative path for RNA agrees well with biochemical data indicating that a 3' single strand overhang of 7-10 nt is necessary for binding and hydrolysis by RNase II [1].
  • We report that mRNA fragments differing from the monocistronic transcript by their 3' termini are also polyadenylated in the absence of polynucleotide phosphorylase and RNase II [6].
  • Similarly, RNase D action on the E. coli tRNATyr precursor is limited, whereas RNase II causes extensive degradation [7].

Chemical compound and disease context of ECs1859

  • The K+-activated diesterase activity against poly(U), which defines RNase II, cochromatographs with activity against T4 mRNA or pulse-labeled E. coli RNA successively on DEAE-cellulose, hydroxyapatite or phosphocellulose, and Sephadex G-150 columns [8].
  • Northern hybridization to rRNA in cells treated with hygromycin B showed that RNase II- and RNase III-deficient strains of E. coli accumulated 16S rRNA fragments upon treatment with the drug [9].
  • The position of modification in the polynucleotide chain was elucidated by comparison of the ribonuclease II/alkaline phosphatase digestion products of the substituted and unsubstituted tRNAPhe samples, and was identified as being exclusively the amino group of the nucleoside X in position 47 of E. coli tRNAPhe [10].

Biological context of ECs1859


Anatomical context of ECs1859


Associations of ECs1859 with chemical compounds

  • However, whereas RNase R shortens RNA processively to di- and trinucleotides, RNase II becomes more distributive when the length of the substrate reaches approximately 10 nucleotides, and it leaves an undigested core of 3-5 nucleotides [13].
  • On denaturing polyacrylamide gels RNase II appears as a single 72,000 dalton species [16].
  • The degradation of poly(C) by RNase II was stimulated by spermine and spermidine, while that of poly(A) by RNase II was not affected by polyamines [17].

Other interactions of ECs1859


Analytical, diagnostic and therapeutic context of ECs1859


  1. Structural Basis for Processivity and Single-Strand Specificity of RNase II. Zuo, Y., Vincent, H.A., Zhang, J., Wang, Y., Deutscher, M.P., Malhotra, A. Mol. Cell (2006) [Pubmed]
  2. Polynucleotide phosphorylase, RNase II and RNase E play different roles in the in vivo modulation of polyadenylation in Escherichia coli. Mohanty, B.K., Kushner, S.R. Mol. Microbiol. (2000) [Pubmed]
  3. Accumulation and turnover of 23S ribosomal RNA in azithromycin-inhibited ribonuclease mutant strains of Escherichia coli. Silvers, J.A., Champney, W.S. Arch. Microbiol. (2005) [Pubmed]
  4. A new role for RNase II in mRNA decay: striking differences between RNase II mutants and similarities with a strain deficient in RNase E. Cruz, A.A., Marujo, P.E., Newbury, S.F., Arraiano, C.M. FEMS Microbiol. Lett. (1996) [Pubmed]
  5. The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold. Bycroft, M., Hubbard, T.J., Proctor, M., Freund, S.M., Murzin, A.G. Cell (1997) [Pubmed]
  6. The rpsO mRNA of Escherichia coli is polyadenylated at multiple sites resulting from endonucleolytic processing and exonucleolytic degradation. Haugel-Nielsen, J., Hajnsdorf, E., Regnier, P. EMBO J. (1996) [Pubmed]
  7. Apparent involvement of ribonuclease D in the 3' processing of tRNA precursors. Cudny, H., Deutscher, M.P. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  8. Purification and some novel properties of Escherichia coli RNase II. Gupta, R.S., Kasai, T., Schlessinger, D. J. Biol. Chem. (1977) [Pubmed]
  9. Hygromycin B Inhibition of Protein Synthesis and Ribosome Biogenesis in Escherichia coli. McGaha, S.M., Champney, W.S. Antimicrob. Agents Chemother. (2007) [Pubmed]
  10. Photolabile and paramagnetic derivatives of the nucleoside X and of Escherichia coli tRNAPhe. Hansske, F., Watanabe, K., Cramer, F., Seela, F. Hoppe-Seyler's Z. Physiol. Chem. (1978) [Pubmed]
  11. Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Donovan, W.P., Kushner, S.R. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  12. Retroregulation of the synthesis of ribosomal proteins L14 and L24 by feedback repressor S8 in Escherichia coli. Mattheakis, L., Vu, L., Sor, F., Nomura, M. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  13. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. Cheng, Z.F., Deutscher, M.P. J. Biol. Chem. (2002) [Pubmed]
  14. Differential sensitivities of portions of the mRNA for ribosomal protein S20 to 3'-exonucleases dependent on oligoadenylation and RNA secondary structure. Coburn, G.A., Mackie, G.A. J. Biol. Chem. (1996) [Pubmed]
  15. The presence of RNase II in high salt washed E. coli ribosomes: effect on circular dichroism of ribosomal complexes. Butzow, J.J., Eichhorn, G.L. Nucleic Acids Res. (1977) [Pubmed]
  16. Amplification of ribonuclease II (rnb) activity in Escherichia coli K-12. Donovan, W.P., Kushner, S.R. Nucleic Acids Res. (1983) [Pubmed]
  17. Effects of polyamines on the activities of Escherichia coli ribonuclease I and II. Kumagai, H., Igarashi, K., Yoshikawa, M., Hirose, S. J. Biochem. (1977) [Pubmed]
  18. The role of endonucleases in the expression of ribonuclease II in Escherichia coli. Zilhão, R., Régnier, P., Arraiano, C.M. FEMS Microbiol. Lett. (1995) [Pubmed]
  19. Expression, purification, crystallization and preliminary diffraction data characterization of Escherichia coli ribonuclease II (RNase II). McVey, C.E., Amblar, M., Barbas, A., Cairrão, F., Coelho, R., Romão, C., Arraiano, C.M., Carrondo, M.A., Frazão, C. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
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